SitesBLAST
Comparing WP_057506694.1 NCBI__GCF_001431535.1:WP_057506694.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q56WD9 3-ketoacyl-CoA thiolase 2, peroxisomal; Acetyl-CoA acyltransferase 2; Beta-ketothiolase 2; Peroxisomal 3-oxoacyl-CoA thiolase 2; Peroxisome defective protein 1; EC 2.3.1.16 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 98% coverage: 7:400/402 of query aligns to 51:437/462 of Q56WD9
- C138 (= C95) modified: Disulfide link with 192
- C192 (≠ A148) modified: Disulfide link with 138
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
43% identity, 99% coverage: 5:400/402 of query aligns to 1:390/392 of P45359
- V77 (≠ D84) mutation to Q: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Y-153 and K-286.
- C88 (= C95) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A103) binding acetate
- N153 (vs. gap) mutation to Y: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and K-286.
- GS 279:280 (≠ SV 289:290) binding acetate
- A286 (≠ E296) mutation to K: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and Y-153.
- C378 (= C388) modified: Disulfide link with 88, In inhibited form
- A386 (= A396) binding acetate
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
45% identity, 98% coverage: 6:400/402 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C95), H346 (= H358), C376 (= C388), G378 (= G390)
- binding acetyl coenzyme *a: C94 (= C95), R214 (= R227), L222 (= L235), L225 (= L238), A238 (= A253), G239 (= G254), S242 (= S257), I244 (≠ M259), A313 (= A328), F314 (= F329), H346 (= H358), C376 (= C388)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 99% coverage: 5:400/402 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C95), H348 (= H358), S378 (≠ C388), G380 (= G390)
- binding coenzyme a: L148 (vs. gap), H156 (≠ G152), R220 (= R227), L231 (= L238), A243 (= A253), S247 (= S257), F319 (= F329), H348 (= H358)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
46% identity, 98% coverage: 7:400/402 of query aligns to 37:420/424 of P09110
- V387 (≠ T368) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
45% identity, 98% coverage: 10:402/402 of query aligns to 7:392/392 of P07097
- Q64 (≠ M70) mutation to A: Slightly lower activity.
- C89 (= C95) mutation to A: Loss of activity.
- C378 (= C388) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C95), H345 (= H358), C375 (= C388), G377 (= G390)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ G152), M154 (= M153), F232 (= F242), S244 (= S257), G245 (≠ Q258), F316 (= F329), H345 (= H358)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C95), H345 (= H358), C375 (= C388), G377 (= G390)
- binding acetyl coenzyme *a: C86 (= C95), L145 (≠ D145), H153 (≠ G152), M154 (= M153), R217 (= R227), S224 (≠ G234), M225 (≠ L235), A240 (= A253), S244 (= S257), M285 (= M298), A315 (= A328), F316 (= F329), H345 (= H358), C375 (= C388)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C95), H345 (= H358), C375 (= C388), G377 (= G390)
- binding coenzyme a: C86 (= C95), L145 (≠ D145), H153 (≠ G152), M154 (= M153), R217 (= R227), L228 (= L238), A240 (= A253), S244 (= S257), H345 (= H358)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 98% coverage: 10:402/402 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C95), H348 (= H358), C378 (= C388), G380 (= G390)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ D145), H156 (≠ G152), M157 (= M153), F235 (= F242), A243 (= A253), S247 (= S257), A318 (= A328), F319 (= F329), H348 (= H358)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 6:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C95), H345 (= H358), C375 (= C388), G377 (= G390)
- binding D-mannose: S6 (≠ A12), A7 (= A13), R38 (≠ Q45), K182 (= K181), D194 (= D193), V280 (= V293), D281 (≠ R294), T287 (≠ I300), P331 (= P344), S332 (= S345), V334 (= V347), V336 (≠ P349), F360 (≠ H373)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
45% identity, 98% coverage: 10:402/402 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C95), H346 (= H358), C376 (= C388), G378 (= G390)
- binding acetoacetyl-coenzyme a: L86 (≠ F94), A87 (≠ C95), L146 (≠ D145), H154 (≠ G152), M155 (= M153), R218 (= R227), S225 (≠ G234), M226 (≠ L235), A241 (= A253), G242 (= G254), S245 (= S257), A316 (= A328), F317 (= F329), H346 (= H358), I377 (= I389), G378 (= G390)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
42% identity, 98% coverage: 10:402/402 of query aligns to 5:375/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (= K23), S89 (≠ C95), M124 (= M130), M146 (= M153), R205 (= R227), T208 (≠ S230), L213 (= L235), L216 (= L238), A226 (= A253), A227 (≠ G254), S229 (= S256), S230 (= S257), M271 (= M298), A301 (= A328), H331 (= H358), L333 (= L360)
P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
40% identity, 99% coverage: 5:401/402 of query aligns to 4:395/397 of P42765
- C92 (= C95) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R227) binding CoA
- T227 (≠ S230) binding CoA
- S251 (= S257) binding CoA
- C382 (= C388) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
40% identity, 99% coverage: 6:402/402 of query aligns to 1:398/400 of 5bz4K
- active site: C87 (= C95), H354 (= H358), C384 (= C388), G386 (= G390)
- binding coenzyme a: C87 (= C95), R146 (≠ P139), M160 (= M153), R220 (= R227), A246 (= A253), G247 (= G254), S250 (= S257), Q252 (≠ M259), M291 (= M298), A321 (= A328), F322 (= F329), H354 (= H358)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 99% coverage: 5:401/402 of query aligns to 7:394/395 of 4c2jD
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:400/402 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C95), A348 (= A355), A378 (≠ V385), L380 (≠ M387)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C95), L151 (≠ V147), A246 (= A253), S250 (= S257), I252 (≠ M259), A321 (= A328), F322 (= F329), H351 (= H358)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:402/402 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C95), H347 (= H358), C377 (= C388), G379 (= G390)
- binding coenzyme a: C88 (= C95), L149 (≠ V147), K219 (≠ R227), F234 (= F242), A242 (= A253), S246 (= S257), A317 (= A328), F318 (= F329), H347 (= H358)
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49 (see paper)
41% identity, 98% coverage: 6:400/402 of query aligns to 2:396/398 of 8oqoC
Query Sequence
>WP_057506694.1 NCBI__GCF_001431535.1:WP_057506694.1
MTKQIQDAYIVAATRTPVGKAPKGVFRNTRPDDMLAHVLRSVVAQAPGIDVNRIDDAIIG
CAMPEAEQGMNVARIGVLLAGLPDTIAAQTVNRFCSSGLQAVAMAADQIRLGNADLMLAG
GTESMSMVPMMGNKIAMAPSVFDNDHVAIAYGMGITAEKVAEEWKVSREEQDAFALASHQ
KAIAAIQNGEFKDEISPYDVRTRQPDLADGRRIITRDKIVDTDEGPRLDSSAEGLAKLRP
VFRNGQFGGTVTAGNSSQMSDGAGAVLLASEQAVKDYGLKPLARFVSFSVAGVRPEVMGI
GPIAAIPKALKQAGLTQDQLDWIELNEAFAAQSLAVIRDCGLDPSKVNPLGGAIALGHPL
GATGAIRTATLLHGLRRRQQKYGMVTMCIGTGMGAAGIFESL
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory